Sunflower trypsin inhibitor-1

Korsinczky, M. L. J., Schirra, H. J. and Craik, D. J. (2004) Sunflower trypsin inhibitor-1. Current Protein & Peptide Science, 5 5: 351-364. doi:10.2174/1389203043379594

Author Korsinczky, M. L. J.
Schirra, H. J.
Craik, D. J.
Title Sunflower trypsin inhibitor-1
Journal name Current Protein & Peptide Science   Check publisher's open access policy
ISSN 1389-2037
Publication date 2004-01-01
Year available 2010
Sub-type Critical review of research, literature review, critical commentary
DOI 10.2174/1389203043379594
Open Access Status Not yet assessed
Volume 5
Issue 5
Start page 351
End page 364
Total pages 14
Place of publication Hilversum
Publisher Bentham Science Publishers
Language eng
Subject C1
Abstract SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K, value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors. It has a cyclic backbone that is cross-braced by a single disulfide bridge and a network of hydrogen bonds that result in a well-defined structure. SFTI-1 is amenable to chemical synthesis, allowing for the creation of synthetic variants. Alterations to the structure such as linearising the backbone or removing the disulfide bridge do not reduce the potency of SFTI-1 significantly, and minimising the peptide to as few as nine residues results in only a small decrease in reactivity. The creation of linear variants of SFTI-1 also provides a tool for investigating putative linear precursor peptides. The mechanism of biosynthesis of SFTI-1 is not yet known but it seems likely that it is a gene-coded product that has arisen from a precursor protein that may be evolutionarily related to classic Bowman-Birk inhibitors.
Keyword Biochemistry & Molecular Biology
Bowman-birk Inhibitor
Circular Backbone
Cyclic Peptide
Reactive-site Loop
Polypeptide Kalata B1
Protease Inhibitor
Serine Proteinases
Q-Index Code C1
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
2005 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 60 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 61 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 15 Aug 2007, 14:38:44 EST